Evidence map›Paper›PMID 29858825›Full record

ReviewJournal of microbiology (Seoul, Korea)2018

Antimicrobial actions of dual oxidases and lactoperoxidase.

Demba Sarr, Eszter Tóth, Aaron Gingerich, Balázs Rada

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of microbiology (Seoul, Korea), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
4.2field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

56 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. Lactoperoxidase is a candidate for mediating neuromelanin formation in the human substantia nigra.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Article
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  12. Review
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  14. To activate NAD(P)H oxidase with a brief pulse of photodynamic action.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
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  16. Review
  17. Article
  18. Review
  19. Article
  20. MedComm · 2024
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Demba SarrDepartment of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, GA, USA.
Eszter TóthDepartment of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, GA, USA.
Aaron GingerichDepartment of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, GA, USA.
Balázs RadaDepartment of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, GA, USA. radab@uga.edu.
University of Georgia · US

Funding

The Role of Oxidative Epithelial Defenses in Influenza InfectionR21AI124189 · NIAID · UNIVERSITY OF GEORGIA · PI RADA, BALAZS, TRIPP, RALPH A · 2017 to 2018
$413k
NIAID NIH HHS R21 AI124189
6 · The paper itself

Abstract

The NOX/DUOX family of NADPH oxidases are transmembrane proteins generating reactive oxygen species as their primary enzymatic products. NADPH oxidase (NOX) 1-5 and Dual oxidase (DUOX) 1 and 2 are members of this family. These enzymes have several biological functions including immune defense, hormone biosynthesis, fertilization, cell proliferation and differentiation, extracellular matrix formation and vascular regulation. They are found in a variety of tissues such as the airways, salivary glands, colon, thyroid gland and lymphoid organs. The discovery of NADPH oxidases has drastically transformed our view of the biology of reactive oxygen species and oxidative stress. Roles of several isoforms including DUOX1 and DUOX2 in host innate immune defense have been implicated and are still being uncovered. DUOX enzymes highly expressed in the respiratory and salivary gland epithelium have been proposed as the major sources of hydrogen peroxide supporting mucosal oxidative antimicrobial defenses. In this review, we shortly present data on DUOX discovery, structure and function, and provide a detailed, up-to-date summary of discoveries regarding antibacterial, antiviral, antifungal, and antiparasitic functions of DUOX enzymes. We also present all the literature describing the immune functions of lactoperoxidase, an enzyme working in partnership with DUOX to produce antimicrobial substances.

Indexed as

AnimalsAntifungal AgentsAnti-Infective AgentsAntiparasitic AgentsAntiviral AgentsDual OxidasesHumansHydrogen PeroxideImmunity, InnateLactoperoxidaseMembrane ProteinsNADPH Oxidase 1NADPH Oxidase 5NADPH OxidasesOxidative StressReactive Oxygen SpeciesAntifungal AgentsAnti-Infective AgentsAntiparasitic AgentsAntiviral AgentsDual OxidasesHydrogen PeroxideLactoperoxidaseMembrane ProteinsNADPH Oxidase 1NADPH Oxidase 5NADPH OxidasesReactive Oxygen SpeciesthiocyanateThiocyanatesantimicrobialdual oxidaseDUOXlactoperoxidaseLPONADPH oxidase

Identifiers

PMID29858825
PMCPMC7336354
OpenAlexW2805722840

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.